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Database: UniProt
Entry: F1L017_ASCSU
LinkDB: F1L017_ASCSU
Original site: F1L017_ASCSU 
ID   F1L017_ASCSU            Unreviewed;       450 AA.
AC   F1L017;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Pachytene checkpoint protein 2 {ECO:0000313|EMBL:ADY43471.1};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY43471.1};
RN   [1] {ECO:0000313|EMBL:ADY43471.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. PCH2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007271}.
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DR   EMBL; JI168840; ADY43471.1; -; mRNA.
DR   AlphaFoldDB; F1L017; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   CDD; cd19508; RecA-like_Pch2-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR044539; Pch2-like.
DR   PANTHER; PTHR45991; PACHYTENE CHECKPOINT PROTEIN 2; 1.
DR   PANTHER; PTHR45991:SF1; PACHYTENE CHECKPOINT PROTEIN 2 HOMOLOG; 1.
DR   Pfam; PF00004; AAA; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003651};
KW   Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003651}.
FT   DOMAIN          202..354
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   450 AA;  50017 MW;  6DE0F3A98D8D87A9 CRC64;
     MNPEKDDTHR RNIDGSDGAV DSRGLAALTD SLSTICIDTT TTFISSIHVE VRLKKGVSKV
     DAEKHRSLVR DALLSLENVV NWRPVPITDE HNLSTLVENI LVGCSASPEG TSLTLTDSSI
     SDANVHFYRI AEYEAEKQEI SADGDPQSAS VGSQMWELPC REFDQIWESL VFDDNIKNEL
     LSYVYALLRI SDRGANSSIL RVNRLILLHG PPGTGKTSLC KGLAQKLSIR LNTRYKQSTF
     VEINSHSLFS KWFSESGKLV QKMFDQIEEL AEDNKTLVFV LIDEVESLSM ARASALSRNE
     PGDAIRAVNA LLTQIDRIRR FPNVLVLATS NISKSLDEAF VDRADMSRFV GQPSVYAVYA
     ILSSCIREMQ RIGIVETTEV IDPLSSYNEF SPNGHRLMQL SRFAVGLSGR ALRQLPVLAY
     SKVALERLTM KQCLEALQKA IEEKKASSCI
//
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